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. 2022 Jan 13;81(4):480–489. doi: 10.1136/annrheumdis-2021-220500

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© Author(s) (or their employer(s)) 2022. Re-use permitted under CC BY-NC. No commercial re-use. See rights and permissions. Published by BMJ.

This is an open access article distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited, appropriate credit is given, any changes made indicated, and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/.

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Molecular model of the three-dimensional structure of the multicomponent DRB1*04:01/Col2 peptide/TCR complex. Superimposition of minimised starting geometries for the trimolecular complexes of TCR#16 with DRB1*04:01 containing either the unmodified (K264) or galactosylated (gal264) version of the Col2_259-273 peptide. The image depicts three side chain bonds irrespective of Col2_259-273 galactosylation: two involving the CDR3 region of the TCRα-chain, Asp94 - Lys264 (Col2_259-273) and Asn97—Glu266 (Col2_259-273) and one in the CDR1 region of the TCRβ-chain, Asp29—Lys270 (Col2_259-273). The galactose (*) residue at Lys264 is not involved in side chain interactions with the TCR. TCR, T-cell receptor.